| Autor: |
BARE, GEORGE H., BROMBERG, PHILIP A., ALBEN, JAMES O., BRIMHALL, BERNADINE, JONES, RICHARD T., MINTZ, SHELDON, ROTHER, IRVING |
| Zdroj: |
Nature; January 1976, Vol. 259 Issue: 5539 p155-156, 2p |
| Abstrakt: |
STUDIES of abnormal human haemoglobins (Hbs) with increased O2affinity have been particularly useful in developing detailed molecular interpretations of normal Hb function. A number of functionally interesting mutants are altered in the βHC region but only one variant, Hb Hiroshima (β146 His→Asp)1,2, has been reported as having a substitution at the C terminus itself. We report here the structure and O2equilibria of Hb York, a new mutation at the β146 position, His→Pro, associated with increased O2affinity, decreased cooperativity and diminished Bohr effect. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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